8BAA

CryoEM structure of GroEL-GroES-ADP.AlF3-Rubisco, class II.

これはPDB形式変換不可エントリーです。

8BAA の概要

• エントリーDOI: 10.2210/pdb8baa/pdb
• EMDBエントリー: 15944
• 分子名称: Chaperonin GroEL, Co-chaperonin GroES, Ribulose bisphosphate carboxylase, ... (7 entities in total)
• 機能のキーワード: groel, groes, chaperone
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 22
• 化学式量合計: 932175.15

構造登録者

Gardner, S.,Saibil, H.R. (登録日: 2022-10-11, 公開日: 2025-02-12, 最終更新日: 2026-02-25)

主引用文献

Gardner, S.,Darrow, M.C.,Lukoyanova, N.,Thalassinos, K.,Saibil, H.R.
Structural basis of substrate progression through the bacterial chaperonin cycle.
Proc.Natl.Acad.Sci.USA, 120:e2308933120-e2308933120, 2023

PubMed Abstract: The bacterial chaperonin GroEL-GroES promotes protein folding through ATP-regulated cycles of substrate protein binding, encapsulation, and release. Here, we have used cryoEM to determine structures of GroEL, GroEL-ADP·BeF, and GroEL-ADP·AlF-GroES all complexed with the model substrate Rubisco. Our structures provide a series of snapshots that show how the conformation and interactions of non-native Rubisco change as it proceeds through the GroEL-GroES reaction cycle. We observe specific charged and hydrophobic GroEL residues forming strong initial contacts with non-native Rubisco. Binding of ATP or ADP·BeF to GroEL-Rubisco results in the formation of an intermediate GroEL complex displaying striking asymmetry in the ATP/ADP·BeF-bound ring. In this ring, four GroEL subunits bind Rubisco and the other three are in the GroES-accepting conformation, suggesting how GroEL can recruit GroES without releasing bound substrate. Our cryoEM structures of stalled GroEL-ADP·AlF-Rubisco-GroES complexes show Rubisco folding intermediates interacting with GroEL-GroES via different sets of residues.

PubMed: 38064510
DOI: 10.1073/pnas.2308933120

実験手法

ELECTRON MICROSCOPY (4.2 Å)